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-Structure paper
| タイトル | Structure of the yeast ceramide synthase. |
|---|---|
| ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 32, Issue 3, Page 441-449, Year 2025 |
| 掲載日 | 2024年11月11日 |
著者 | Jan-Hannes Schäfer / Lena Clausmeyer / Carolin Körner / Bianca M Esch / Verena N Wolf / Jennifer Sapia / Yara Ahmed / Stefan Walter / Stefano Vanni / Dovile Januliene / Arne Moeller / Florian Fröhlich / ![]() |
| PubMed 要旨 | Ceramides are essential lipids involved in forming complex sphingolipids and acting as signaling molecules. They result from the N-acylation of a sphingoid base and a CoA-activated fatty acid, a ...Ceramides are essential lipids involved in forming complex sphingolipids and acting as signaling molecules. They result from the N-acylation of a sphingoid base and a CoA-activated fatty acid, a reaction catalyzed by the ceramide synthase (CerS) family of enzymes. Yet, the precise structural details and catalytic mechanisms of CerSs have remained elusive. Here we used cryo-electron microscopy single-particle analysis to unravel the structure of the yeast CerS complex in both an active and a fumonisin B1-inhibited state. Our results reveal the complex's architecture as a dimer of Lip1 subunits bound to the catalytic subunits Lag1 and Lac1. Each catalytic subunit forms a hydrophobic crevice connecting the cytosolic site with the intermembrane space. The active site, located centrally in the tunnel, was resolved in a substrate preloaded state, representing one intermediate in ceramide synthesis. Our data provide evidence for competitive binding of fumonisin B1 to the acyl-CoA-binding tunnel. |
リンク | Nat Struct Mol Biol / PubMed:39528796 |
| 手法 | EM (単粒子) |
| 解像度 | 3.0 - 3.2 Å |
| 構造データ | EMDB-18652, PDB-8qtn: EMDB-18653, PDB-8qtr: |
| 化合物 | ![]() ChemComp-3PE: ![]() ChemComp-7PO: ![]()
ChemComp-PIJ: ![]() ChemComp-NH4: ![]()
ChemComp-WXE: |
| 由来 |
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キーワード | MEMBRANE PROTEIN / Ceramide Synthase |
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